|Other Names||ATP-dependent RNA helicase DDX19B, DEAD box RNA helicase DEAD5, DEAD box protein 19B, DDX19B, DBP5, DDX19, TDBP|
|Target/Specificity||The synthetic peptide sequence is selected from aa 22-36 of HUMAN DDX19B|
|Format||Synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml DI water for a final concentration of 1 mg/ml.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.|
|Precautions||This product is for research use only. Not for use in diagnostic or therapeutic procedures.|
|Synonyms||DBP5, DDX19, TDBP|
|Function||ATP-dependent RNA helicase involved in mRNA export from the nucleus. Rather than unwinding RNA duplexes, DDX19B functions as a remodeler of ribonucleoprotein particles, whereby proteins bound to nuclear mRNA are dissociated and replaced by cytoplasmic mRNA binding proteins.|
|Cellular Location||Cytoplasm. Nucleus, nuclear pore complex. Nucleus membrane; Peripheral membrane protein; Cytoplasmic side Note=Nuclear pore complex cytoplasmic fibrils|
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Provided below are standard protocols that you may find useful for product applications.
DEAD box proteins, characterized by the conserved motif Asp-Glu-Ala-Asp (DEAD), are putative RNA helicases. They are implicated in a number of cellular processes involving alteration of RNA secondary structure such as translation initiation, nuclear and mitochondrial splicing, and ribosome and spliceosome assembly. Based on their distribution patterns, some members of this family are believed to be involved in embryogenesis, spermatogenesis, and cellular growth and division. This gene encodes a DEAD box protein, which exhibits RNA-dependent ATPase and ATP-dependent RNA-unwinding activities. This protein is recruited to the cytoplasmic fibrils of the nuclear pore complex, where it participates in the export of mRNA from the nucleus. Multiple alternatively spliced transcript variants encoding different isoforms have been found for this gene.
Collins, R., et al. J. Biol. Chem. 284(16):10296-10300(2009)
von Moeller, H., et al. Nat. Struct. Mol. Biol. 16(3):247-254(2009)
Lamesch, P., et al. Genomics 89(3):307-315(2007)
Ewing, R.M., et al. Mol. Syst. Biol. 3, 89 (2007) :
Yin, L., et al. Reprod. Fertil. Dev. 14 (3-4), 185-189 (2002) :
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